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A0A7G3UCL8 · A0A7G3UCL8_STRT9

Function

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Pathway

Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.

Features

Showing features for binding site.

130820406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site98substrate
Binding site135FAD (UniProtKB | ChEBI)
Binding site163FAD (UniProtKB | ChEBI)
Binding site187-189FAD (UniProtKB | ChEBI)
Binding site201FAD (UniProtKB | ChEBI)
Binding site226-227FAD (UniProtKB | ChEBI)
Binding site288substrate
Binding site289substrate

GO annotations

AspectTerm
Molecular Functionnucleotide binding
Molecular Functionproline dehydrogenase activity
Biological Processproline catabolic process to glutamate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    proline dehydrogenase
  • EC number

Gene names

    • ORF names
      STSU_009155

Organism names

Accessions

  • Primary accession
    A0A7G3UCL8

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain46-299Proline dehydrogenase

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    308
  • Mass (Da)
    34,137
  • Last updated
    2021-02-10 v1
  • MD5 Checksum
    6DF62CB9C85D96E244D26620A7C0121D
MLGPVILAASRSDKMRRVISAAPVTKPVVNRFIAGETVDETVPVVRDSAARGLEVTLDVLGEDITDASEALRARDAYLELIEALKPLGLGERAEMSVKLSSFGQALPGGHDLALKNVTPVVEAAAEIGTTVTLDMEDHTTVDSTLAIHAELRERFPRTGAVVQSYLFRTEDDCRMLAEAGSRVRLVKGAYKEPASVAYQNKAEVDKAYIRCLRILMEGEGYPMIGSHDPRIISITQELARRAGRKLDDYEFQMLYGIREAEQARLAAEGHRMRLYIAYGTDWYGYFMRRLAERPANLAFFLRSLATRG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP029159
EMBL· GenBank· DDBJ
QKM67311.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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